Cited by 306Hemoglobinopathies and Related DisordersHemoglobin structure and functionBlood properties and coagulation

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Accelerated autoxidation and heme loss due to instability of sickle hemoglobin.

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Hebbel, R P, Morgan, W T, Eaton, J W, Hedlund, B E·1988·Proceedings of the National Academy of Sciences

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Abstract

The pleiotropic effect of the sickle gene suggests that factors in addition to polymerization of the mutant gene product might be involved in sickle disease pathobiology. We have examined rates of heme transfer to hemopexin from hemoglobin in dilute aqueous solution (0.5 mg of Hb per ml) at 37 degrees C. HbO2 S loses heme 1.7 times faster than HbO2 A, with apparent rate constants of 0.024 hr-1 and 0.014 hr-1, respectively. In contrast, Hb A and Hb S behave identically in their MetHb forms (very rapid heme loss) and their HbCO forms (zero heme loss). This indicates that the faster heme loss from HbO2 S is due to accelerated autoxidation (HbO2----MetHb) rather than to some other type of instability inherent in the relationship of sickle heme to its pocket in globin. This interpretation is supported by spectrophotometric measurement of initial rates of MetHb formation during incubation at 37 degrees C. This directly shows 1.7 times faster autoxidation, with apparent rate constants of 0.050 hr-1 for HbO2 S and 0.029 hr-1 for HbO2 A. While the participation of this process in the cellular pathobiology of sickle erythrocytes remains unproven, the present data are consistent with, and perhaps help explain, two prior observations: the excessive spontaneous generation of superoxide by sickle erythrocytes; and the abnormal deposition of heme and heme proteins on membranes of sickle erythrocytes.

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Authors: Hebbel, R. P., Morgan, W. T., Eaton, J. W., & Hedlund, B. E.
Affiliations: University of Minnesota (US)
ORCID: Hebbel, R P
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 1988-01
Volume: 85
Issue: 1
Pages: 237-241
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.85.1.237
PMC: PMC279519
OpenAlex: W2019673916
Cited by: 306
References: 24
Citations by year: 2026: 3 · 2025: 6 · 2024: 4 · 2023: 6 · 2022: 14 · 2021: 12 · 2020: 13 · 2019: 20 · 2018: 13 · 2017: 17 · 2016: 12 · 2015: 13 · 2014: 11 · 2013: 18 · 2012: 5
FWCI: 4.97
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Heart, Lung, and Blood Institute (HL01130, HL30160)
National Institute of Diabetes and Digestive and Kidney Diseases (DK 27237)
Topics: Health Sciences › Medicine › Genetics (clinical) › Hemoglobinopathies and Related Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
Health Sciences › Medicine › Hematology › Blood properties and coagulation
Keywords: hemoglobin S, heme loss, autoxidation, methemoglobin formation, hemopexin, superoxide production, sickle erythrocytes
MeSH terms: Anemia, Sickle Cell, Drug Stability, Heme, Hemoglobin A, Hemoglobin, Sickle, Humans, Kinetics, Oxidation-Reduction, Reference Values, Spectrophotometry

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Accelerated autoxidation and heme loss due to instability of sickle hemoglobin.

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